|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
1-448 |
0e+00 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 814.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 1 MKPLLLTNALIINEDLRYPADILIDKGRIQKIASLIPSRTEWQVIDVRGKWVIPGMIDDQVHFREPGLTHKGTIASESAA 80
Cdd:PRK09236 1 MKRILIKNARIVNEGKIFEGDVLIENGRIAKIASSISAKSADTVIDAAGRYLLPGMIDDQVHFREPGLTHKGDIASESRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 81 AVMGGITSFMEMPNVTPPTTTLQALREKFQRASHSSLANYSFYFGATNDNLDELKALTASQACGVKVFMGASTGNMLVDD 160
Cdd:PRK09236 81 AVAGGITSFMEMPNTNPPTTTLEALEAKYQIAAQRSLANYSFYFGATNDNLDEIKRLDPKRVCGVKVFMGASTGNMLVDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 161 EQILESIFANAPCLVATHCEHTPTIKHNEETWRARLGDAIPAGEHAAIRSVDACLTSSHQAVSLAKKHRTRLHVLHITTA 240
Cdd:PRK09236 161 PETLERIFRDAPTLIATHCEDTPTIKANLAKYKEKYGDDIPAEMHPLIRSAEACYKSSSLAVSLAKKHGTRLHVLHISTA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 241 DELALFDAAPtleaLRQKTITTEACVHHLFFNYDDYEMLGHKLKCNPSVKSSFHQEALWRGVNEGIIDVIATDHAPHLLE 320
Cdd:PRK09236 241 KELSLFENGP----LAEKRITAEVCVHHLWFDDSDYARLGNLIKCNPAIKTASDREALRQALADDRIDVIATDHAPHTWE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 321 EKQNDYFAAPSGLPLVQHALPALLDMSSRGIFTPEMVVRKTSHAVAERFQLKDRGYIREGYWADLVVIDPFSHQQIIRED 400
Cdd:PRK09236 317 EKQGPYFQAPSGLPLVQHALPALLELVHEGKLSLEKVVEKTSHAPAILFDIKERGFIREGYWADLVLVDLNSPWTVTKEN 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1456770152 401 VAYKCGWSPFEGRILSgGAVDMTLVNGHVIWNGRTIQQKY-GLPLEFCR 448
Cdd:PRK09236 397 ILYKCGWSPFEGRTFR-SRVATTFVNGQLVYHNGQLVESCrGQRLEFDR 444
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
5-446 |
9.58e-174 |
|
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; Dihydroorotase or related cyclic amidohydrolase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 439814 [Multi-domain] Cd Length: 439 Bit Score: 493.84 E-value: 9.58e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 5 LLTNALIINEDLRYPADILIDKGRIQKIASLIPSRTEWQVIDVRGKWVIPGMIDDQVHFREPGLTHKGTIASESAAAVMG 84
Cdd:COG0044 1 LIKNGRVVDPGGLERADVLIEDGRIAAIGPDLAAPEAAEVIDATGLLVLPGLIDLHVHLREPGLEHKEDIETGTRAAAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 85 GITSFMEMPNVTPPTTTLQALREKFQRASHSSLANYSFYFGATND---NLDELKALTASQACGVKVFMGASTGNMLVDDE 161
Cdd:COG0044 81 GVTTVVDMPNTNPVTDTPEALEFKLARAEEKALVDVGPHGALTKGlgeNLAELGALAEAGAVAFKVFMGSDDGNPVLDDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 162 QILEsIFANA---PCLVATHCEHTPTIKH---NEETWRARLgdaipageHAAIRSVDACLTSSHQAVSLAKKHRTRLHVL 235
Cdd:COG0044 161 LLRR-ALEYAaefGALVAVHAEDPDLIRGgvmNEGKTSPRL--------GLKGRPAEAEEEAVARDIALAEETGARLHIV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 236 HITTADELALFDAAPtleaLRQKTITTEACVHHLFFNYDDYEMLGHKLKCNPSVKSSFHQEALWRGVNEGIIDVIATDHA 315
Cdd:COG0044 232 HVSTAEAVELIREAK----ARGLPVTAEVCPHHLTLTDEDLERYGTNFKVNPPLRTEEDREALWEGLADGTIDVIATDHA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 316 PHLLEEKQNDYFAAPSGLPLVQHALPALLD-MSSRGIFTPEMVVRKTSHAVAERFQLKDRGYIREGYWADLVVIDPFSHQ 394
Cdd:COG0044 308 PHTLEEKELPFAEAPNGIPGLETALPLLLTeLVHKGRLSLERLVELLSTNPARIFGLPRKGRIAVGADADLVLFDPDAEW 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1456770152 395 QIIREDVAYKCGWSPFEGRILSgGAVDMTLVNGHVIW-NGRTIQQKYGLPLEF 446
Cdd:COG0044 388 TVTAEDLHSKSKNTPFEGRELT-GRVVATIVRGRVVYeDGEVVGEPRGRFLRR 439
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
1-446 |
8.88e-157 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 450.67 E-value: 8.88e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 1 MKPLLLTNALII--NEDLrYPADILIDKGRIQKIASLIPSRTEWQVIDVRGKWVIPGMIDDQVHFREPGLTHKGTIASES 78
Cdd:PRK07575 2 MMSLLIRNARILlpSGEL-LLGDVLVEDGKIVAIAPEISATAVDTVIDAEGLTLLPGVIDPQVHFREPGLEHKEDLFTAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 79 AAAVMGGITSFMEMPNVTPPTTTLQALREKFQRASHSSLANYSFYFGATNDNLDELkaLTASQACGVKVFMGASTGNMLV 158
Cdd:PRK07575 81 RACAKGGVTSFLEMPNTKPLTTTQAALDDKLARAAEKCVVNYGFFIGATPDNLPEL--LTANPTCGIKIFMGSSHGPLLV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 159 DDEQILESIFANAPCLVATHCEHTPTIKHNeetwRARL-GDAIPAgEHAAIRSVDACLTSSHQAVSLAKKHRTRLHVLHI 237
Cdd:PRK07575 159 DEEAALERIFAEGTRLIAVHAEDQARIRAR----RAEFaGISDPA-DHSQIQDEEAALLATRLALKLSKKYQRRLHILHL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 238 TTADELalfdaaptlEALRQKT---ITTEACVHHLFFNYDDYEMLGHKLKCNPSVKSSFHQEALWRGVNEGIIDVIATDH 314
Cdd:PRK07575 234 STAIEA---------ELLRQDKpswVTAEVTPQHLLLNTDAYERIGTLAQMNPPLRSPEDNEALWQALRDGVIDFIATDH 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 315 APHLLEEKQNDYFAAPSGLPLVQHALPALLDMSSRGIFTPEMVVRKTSHAVAERFQLKDRGYIREGYWADLVVIDPFSHQ 394
Cdd:PRK07575 305 APHTLEEKAQPYPNSPSGMPGVETSLPLMLTAAMRGKCTVAQVVRWMSTAVARAYGIPNKGRIAPGYDADLVLVDLNTYR 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1456770152 395 QIIREDVAYKCGWSPFEGRILSGGAVdMTLVNGHVIW-NGRTIQQKYGLPLEF 446
Cdd:PRK07575 385 PVRREELLTKCGWSPFEGWNLTGWPV-TTIVGGQIVFdRGQVNTEVRGQALTF 436
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
49-427 |
1.36e-148 |
|
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis. This group contains the archeal members of the DHOase family.
Pssm-ID: 238643 [Multi-domain] Cd Length: 361 Bit Score: 427.14 E-value: 1.36e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 49 GKWVIPGMIDDQVHFREPGLTHKGTIASESAAAVMGGITSFMEMPNVTPPTTTLQALREKFQRASHSSLANYSFYFGATN 128
Cdd:cd01318 1 GLLILPGVIDIHVHFREPGLTYKEDFVSGSRAAAAGGVTTVMDMPNTKPPTTTAEALYEKLRLAAAKSVVDYGLYFGVTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 129 DnlDELKALTASQACGVKVFMGASTGNMLvDDEQILESIFANAPCLVATHCEHTPTIKHNEETWRARlgdaipaGEHAAI 208
Cdd:cd01318 81 S--EDLEELDKAPPAGYKIFMGDSTGDLL-DDEETLERIFAEGSVLVTFHAEDEDRLRENRKELKGE-------SAHPRI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 209 RSVDACLTSSHQAVSLAKKHRTRLHVLHITTADELALFDAAPtlealrqKTITTEACVHHLFFNYDDYEMLGHKLKCNPS 288
Cdd:cd01318 151 RDAEAAAVATARALKLARRHGARLHICHVSTPEELKLIKKAK-------PGVTVEVTPHHLFLDVEDYDRLGTLGKVNPP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 289 VKSSFHQEALWRGVNEGIIDVIATDHAPHLLEEKQNDYFAAPSGLPLVQHALPALLDMSSRGIFTPEMVVRKTSHAVAER 368
Cdd:cd01318 224 LRSREDRKALLQALADGRIDVIASDHAPHTLEEKRKGYPAAPSGIPGVETALPLMLTLVNKGILSLSRVVRLTSHNPARI 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1456770152 369 FQLKDRGYIREGYWADLVVIDPFSHQQIIREDVAYKCGWSPFEGRILSGGaVDMTLVNG 427
Cdd:cd01318 304 FGIKNKGRIAEGYDADLTVVDLKEERTIRAEEFHSKAGWTPFEGFEVTGF-PVMTIVRG 361
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
4-446 |
2.28e-127 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 376.18 E-value: 2.28e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 4 LLLTNALIINEDLRYPADILIDKGRIQKIASLIPSRTEwQVIDVRGKWVIPGMIDDQVHFREPGLTHKGTIASESAAAVM 83
Cdd:PRK09060 7 LILKGGTVVNPDGEGRADIGIRDGRIAAIGDLSGASAG-EVIDCRGLHVLPGVIDSQVHFREPGLEHKEDLETGSRAAVL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 84 GGITSFMEMPNVTPPTTTLQALREKFQRASHSSLANYSFYFGATNDNLDELKAL-TASQACGVKVFMGASTGNMLVDDEQ 162
Cdd:PRK09060 86 GGVTAVFEMPNTNPLTTTAEALADKLARARHRMHCDFAFYVGGTRDNADELAELeRLPGCAGIKVFMGSSTGDLLVEDDE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 163 ILESIFANAPCLVATHCEHtptikhnEETWRARLGDAIP--AGEHAAIRSVDACLTSSHQAVSLAKKHRTRLHVLHITTA 240
Cdd:PRK09060 166 GLRRILRNGRRRAAFHSED-------EYRLRERKGLRVEgdPSSHPVWRDEEAALLATRRLVRLARETGRRIHVLHVSTA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 241 DELALfdaaptleaLRQ-KTITT-EACVHHLFFNYDD-YEMLGHKLKCNPSVKSSFHQEALWRGVNEGIIDVIATDHAPH 317
Cdd:PRK09060 239 EEIDF---------LADhKDVATvEVTPHHLTLAAPEcYERLGTLAQMNPPIRDARHRDGLWRGVRQGVVDVLGSDHAPH 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 318 LLEEKQNDYFAAPSGLPLVQHALPALLDMSSRGIFTPEMVVRKTSHAVAERFQLKDRGYIREGYWADLVVIDPFSHQQII 397
Cdd:PRK09060 310 TLEEKAKPYPASPSGMTGVQTLVPIMLDHVNAGRLSLERFVDLTSAGPARIFGIAGKGRIAVGYDADFTIVDLKRRETIT 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1456770152 398 REDVAYKCGWSPFEGRILSGGAVdMTLVNGH-VIWNGRTIQQKYGLPLEF 446
Cdd:PRK09060 390 NEWIASRCGWTPYDGKEVTGWPV-GTIVRGQrVMWDGELVGPPTGEPVRF 438
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
1-441 |
8.26e-106 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 320.83 E-value: 8.26e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 1 MKPLLLTNALIINEDLRYPADILIDKGRIQKIASLIPSRTEWQVIDVRGKWVIPGMIDDQVHFREPGLTHKGTIASESAA 80
Cdd:PRK02382 1 MRDALLKDGRVYYNNSLQPRDVRIDGGKITAVGKDLDGSSSEEVIDARGMLLLPGGIDVHVHFREPGYTHKETWYTGSRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 81 AVMGGITSFMEMPNVTPPTTTLQALREKFQRASHSSLANYSFYFGATN--DNLDELKALTASqACGvKVFMGASTGNMLV 158
Cdd:PRK02382 81 AAAGGVTTVVDQPNTDPPTVDGESFDEKAELAARKSIVDFGINGGVTGnwDPLESLWERGVF-ALG-EIFMADSTGGMGI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 159 DdEQILESIFANAPCLVATHCEHTPTIKHNEETWRARLGDAIPAGeHAAIRSVDACLTSSHQAVSLAKKHRTRLHVLHIT 238
Cdd:PRK02382 159 D-EELFEEALAEAARLGVLATVHAEDEDLFDELAKLLKGDADADA-WSAYRPAAAEAAAVERALEVASETGARIHIAHIS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 239 TADelalfdaapTLEALRQKTITTEACVHHLFFNYDDYEMLGHKLKCNPSVKSSFHQEALWRGVNEGIIDVIATDHAPHL 318
Cdd:PRK02382 237 TPE---------GVDAARREGITCEVTPHHLFLSRRDWERLGTFGKMNPPLRSEKRREALWERLNDGTIDVVASDHAPHT 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 319 LEEKQNDYFAAPSGLPLVQHALPALLDMSSRGIFTPEMVVRKTSHAVAERFQLKDRGYIREGYWADLVVIDPFSHQQIIR 398
Cdd:PRK02382 308 REEKDADIWDAPSGVPGVETMLPLLLAAVRKNRLPLERVRDVTAANPARIFGLDGKGRIAEGYDADLVLVDPDAAREIRG 387
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1456770152 399 EDVAYKCGWSPFEGriLSGGAVDMTLVNGHVIWNGRTIQQKYG 441
Cdd:PRK02382 388 DDLHSKAGWTPFEG--MEGVFPELTMVRGTVVWDGDDINAKRG 428
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
4-432 |
3.68e-89 |
|
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the dihydropyrimidinase family, which catalyzes the reversible hydrolytic ring opening of dihydropyrimidines and hydantoins (five-membered cyclic diamides used in biotechnology). But L-HYDs differ by having an L-enantio specificity and by lacking activity on possible natural substrates such as dihydropyrimidines. Allantoinase catalyzes the hydrolytic cleavage of the five-member ring of allantoin (5-ureidohydantoin) to form allantoic acid.
Pssm-ID: 238640 [Multi-domain] Cd Length: 447 Bit Score: 278.40 E-value: 3.68e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 4 LLLTNALIINEDLRYPADILIDKGRIQKIASLIPSRTEWQVIDVRGKWVIPGMIDDQVHFREPGLTHKGTIASESAAAVM 83
Cdd:cd01315 2 LVIKNGRVVTPDGVREADIAVKGGKIAAIGPDIANTEAEEVIDAGGLVVMPGLIDTHVHINEPGRTEWEGFETGTKAAAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 84 GGITSFMEMP-NVTPPTTTLQALREKFQRASHSSLANYSFYFGATNDNLDELKALTASQACGVKVFMGASTGNML--VDD 160
Cdd:cd01315 82 GGITTIIDMPlNSIPPTTTVENLEAKLEAAQGKLHVDVGFWGGLVPGNLDQLRPLDEAGVVGFKCFLCPSGVDEFpaVDD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 161 EQILE--SIFANAPCLVATHCEHTPTIKhnEETWRARLGDAIPAGEHAAIRSVDACLTSSHQAVSLAKKHRTRLHVLHIT 238
Cdd:cd01315 162 EQLEEamKELAKTGSVLAVHAENPEITE--ALQEQAKAKGKRDYRDYLASRPVFTEVEAIQRILLLAKETGCRLHIVHLS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 239 TAdelalfDAAPTLEALRQK--TITTEACVHHLFFNYDDYEMLGHKLKCNPSVKSSFHQEALWRGVNEGIIDVIATDHAP 316
Cdd:cd01315 240 SA------EAVPLIREARAEgvDVTVETCPHYLTFTAEDVPDGGTEFKCAPPIRDAANQEQLWEALENGDIDMVVSDHSP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 317 HLLEEK---QNDYFAAPSGLPLVQHALPALLDM-SSRGIFTPEMVVRKTSHAVAERFQLKDR-GYIREGYWADLVVIDPF 391
Cdd:cd01315 314 CTPELKllgKGDFFKAWGGISGLQLGLPVMLTEaVNKRGLSLEDIARLMCENPAKLFGLSHQkGRIAVGYDADFVVWDPE 393
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1456770152 392 SHQQIIREDVAYKCGWSPFEGRILsGGAVDMTLVNGHVIWN 432
Cdd:cd01315 394 EEFTVDAEDLYYKNKISPYVGRTL-KGRVHATILRGTVVYQ 433
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
20-429 |
1.18e-87 |
|
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of dihydroorotase found in E. coli, this class tends to appear in a large, multifunctional complex with aspartate transcarbamoylase. Homologous domains appear in multifunctional proteins of higher eukaryotes. In some species, including Pseudomonas putida and P. aeruginosa, this protein is inactive but is required as a non-catalytic subunit of aspartate transcarbamoylase (ATCase). In these species, a second, active dihydroorotase is also present. The seed for this model does not include any example of the dihydroorotase domain of eukaryotic multidomain pyrimidine synthesis proteins. All proteins described by this model should represent active and inactive dihydroorotase per se and functionally equivalent domains of multifunctional proteins from higher eukaryotes, but exclude related proteins such as allantoinase. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273302 [Multi-domain] Cd Length: 411 Bit Score: 273.16 E-value: 1.18e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 20 ADILIDKGRIQKIASLIPSRTEwQVIDVRGKWVIPGMIDDQVHFREPGLTHKGTIASESAAAVMGGITSFMEMPNVTPPT 99
Cdd:TIGR00857 6 VDILVEGGRIKKIGKLRIPPDA-EVIDAKGLLVLPGFIDLHVHLRDPGEEYKEDIESGSKAAAHGGFTTVADMPNTKPPI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 100 TTLQALREKFQRASHSSLANYSFYFGATNDNldELKALTASqacgVKVFMGASTGNMLVDD---------EQILESIFAN 170
Cdd:TIGR00857 85 DTPETLEWKLQRLKKVSLVDVHLYGGVTQGN--QGKELTEA----YELKEAGAVGRMFTDDgsevqdilsMRRALEYAAI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 171 APCLVATHCEHTPTI---KHNEETWRARLGDAI--PAGEHAAIRSVdacltsshqaVSLAKKHRTRLHVLHITTADELAL 245
Cdd:TIGR00857 159 AGVPIALHAEDPDLIyggVMHEGPSAAQLGLPArpPEAEEVAVARL----------LELAKHAGCPVHICHISTKESLEL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 246 fdaaptLEALRQK--TITTEACVHHLFFNYDDYEMLGHKLKCNPSVKSSFHQEALWRGVNEGIIDVIATDHAPHLLEEKQ 323
Cdd:TIGR00857 229 ------IVKAKSQgiKITAEVTPHHLLLSEEDVARLDGNGKVNPPLREKEDRLALIEGLKDGIIDIIATDHAPHTLEEKT 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 324 NDYFAAPSGLPLVQHALPALLDMSSRGIFTPEMVVRKTSHAVAERFQLKDRGYIREGYWADLVVIDPFSHQQIIREDVAY 403
Cdd:TIGR00857 303 KEFAAAPPGIPGLETALPLLLQLLVKGLISLKDLIRMLSINPARIFGLPDKGTLEEGNPADITVFDLKKEWTINAETFYS 382
|
410 420
....*....|....*....|....*.
gi 1456770152 404 KCGWSPFEGRILSGGaVDMTLVNGHV 429
Cdd:TIGR00857 383 KAKNTPFEGMSLKGK-PIATILRGKV 407
|
|
| allantoinase |
TIGR03178 |
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ... |
4-436 |
8.26e-80 |
|
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ring-opening hydrolysis. The seed members of this model are all in the vicinity of other genes involved in the processes of xanthine/urate/allantoin catabolism. Although not included in the seed, many eukaryotic homologs of this family are included above the trusted cutoff. Below the noise cutoff are related hydantoinases.
Pssm-ID: 163175 [Multi-domain] Cd Length: 443 Bit Score: 253.84 E-value: 8.26e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 4 LLLTNALIINEDLRYPADILIDKGRIQKIASlIPSRTEWQVIDVRGKWVIPGMIDDQVHFREPGLTHKGTIASESAAAVM 83
Cdd:TIGR03178 2 LIIRGGRVILPNGEREADVGVKGGKIAAIGP-DILGPAAKIIDAGGLVVFPGVVDTHVHINEPGRTEWEGFETGTRAAAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 84 GGITSFMEMP-NVTPPTTTLQALREKFQRASHSSLANYSFYFGATNDNLDELKALTASQACGVKVFMGASTGN--MLVDD 160
Cdd:TIGR03178 81 GGITTYIDMPlNSIPATTTRASLEAKFEAAKGKLAVDVGFWGGLVPYNLDDLRELDEAGVVGFKAFLSPSGDDefPHVDD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 161 EQILES--IFANAPCLVATHCEhTPTIkHNEETWRARLGDAIPAGEHAAIRSVDACLTSSHQAVSLAKKHRTRLHVLHIT 238
Cdd:TIGR03178 161 WQLYKGmrELARLGQLLLVHAE-NPAI-TSALGEEAPPQGGVGADAYLASRPVFAEVEAIRRTLALAKVTGCRVHVVHLS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 239 TADELALFDAAptlealRQK--TITTEACVHHLFFNYDDYEMLGHKLKCNPSVKSSFHQEALWRGVNEGIIDVIATDHAP 316
Cdd:TIGR03178 239 SAEAVELITEA------KQEglDVTVETCPHYLTLTAEEVPDGGTLAKCAPPIRDLANQEGLWEALLNGLIDCVVSDHSP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 317 HLLEEKQ-NDYFAAPSGLPLVQHALPALLD--MSSRGIfTPEMVVRKTSHAVAERFQLKDRGYIREGYWADLVVIDPFSH 393
Cdd:TIGR03178 313 CTPDLKRaGDFFKAWGGIAGLQSTLDVMFDeaVQKRGL-PLEDIARLMATNPAKRFGLAQKGRIAPGKDADFVFVDPDES 391
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1456770152 394 QQIIREDVAYKCGWSPFEGRILsGGAVDMTLVNGHVIWNGRTI 436
Cdd:TIGR03178 392 YTLTPDDLYYRHKVSPYVGRTI-GGRVRATYLRGQCIYDDEQF 433
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
4-431 |
2.42e-79 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 252.04 E-value: 2.42e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 4 LLLTNALIIN-EDLRYPADILIDKGRIQKIASLIPSRTEwQVIDVRGKWVIPGMIDDQVHFREPGLTHKGTIASESAAAV 82
Cdd:PRK09357 3 ILIKNGRVIDpKGLDEVADVLIDDGKIAAIGENIEAEGA-EVIDATGLVVAPGLVDLHVHLREPGQEDKETIETGSRAAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 83 MGGITSFMEMPNVTPPTTTLQALREKFQRASHSSLANY----SFYFGATNDNLDELKALTASqacGVKVFmgaSTGNMLV 158
Cdd:PRK09357 82 AGGFTTVVAMPNTKPVIDTPEVVEYVLDRAKEAGLVDVlpvgAITKGLAGEELTEFGALKEA---GVVAF---SDDGIPV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 159 DDEQILESIFANAP---CLVATHCEHTPTIKH---NEETWRARLGDA-IPAGEHAAIRSVDacltsshqaVSLAKKHRTR 231
Cdd:PRK09357 156 QDARLMRRALEYAKaldLLIAQHCEDPSLTEGgvmNEGEVSARLGLPgIPAVAEEVMIARD---------VLLAEATGAR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 232 LHVLHITTADelalfdaapTLEALRQ-K----TITTEACVHHLFFNYDDYEMLGHKLKCNPSVKSSFHQEALWRGVNEGI 306
Cdd:PRK09357 227 VHICHVSTAG---------SVELIRWaKalgiKVTAEVTPHHLLLTDEDLLTYDPNYKVNPPLRTEEDREALIEGLKDGT 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 307 IDVIATDHAPHLLEEKQNDYFAAPSGLPLVQHALPALLD-MSSRGIFTPEMVVRKTSHAVAERFQLKDrGYIREGYWADL 385
Cdd:PRK09357 298 IDAIATDHAPHAREEKECEFEAAPFGITGLETALSLLYTtLVKTGLLDLEQLLEKMTINPARILGLPA-GPLAEGEPADL 376
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1456770152 386 VVIDPFSHQQIIREDVAYKCGWSPFEGRILSgGAVDMTLVNGHVIW 431
Cdd:PRK09357 377 VIFDPEAEWTVDGEDFASKGKNTPFIGMKLK-GKVVYTIVDGKIVY 421
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
4-432 |
1.08e-78 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 251.16 E-value: 1.08e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 4 LLLTNALIINEDLRYPADILIDKGRIQKIASLIPSRTEwQVIDVRGKWVIPGMIDDQVHFREPGLTHKGTIASESAAAVM 83
Cdd:PRK06189 5 LIIRGGKVVTPEGVYRADIGIKNGKIAEIAPEISSPAR-EIIDADGLYVFPGMIDVHVHFNEPGRTHWEGFATGSAALAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 84 GGITSFMEMP-NVTPPTTTLQALREKFQRASHSSLANYSFYFGATNDNLDELKALTASQACGVKVFMGASTGNML--VDD 160
Cdd:PRK06189 84 GGCTTYFDMPlNSIPPTVTREALDAKAELARQKSAVDFALWGGLVPGNLEHLRELAEAGVIGFKAFMSNSGTDEFrsSDD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 161 EQILESIFANAPC--LVATHCEHTPTIKHNEETWRARLGDAIPAgeHAAIRSVDACLTSSHQAVSLAKKHRTRLHVLHIT 238
Cdd:PRK06189 164 LTLYEGMKEIAALgkILALHAESDALTRHLTTQARQQGKTDVRD--YLESRPVVAELEAVQRALLYAQETGCPLHFVHIS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 239 TADELALFDAAPTlealRQKTITTEACVHHLFFNYDDYEMLGHKLKCNPSVKSSFHQEALWRGVNEGIIDVIATDHAPHL 318
Cdd:PRK06189 242 SGKAVALIAEAKK----RGVDVSVETCPHYLLFTEEDFERIGAVAKCAPPLRSRSQKEELWRGLLAGEIDMISSDHSPCP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 319 LEEK-QNDYFAAPSGLPLVQHALPALLDMS--SRGIfTPEMVVRKTSHAVAERFQLKDRGYIREGYWADLVVIDPFSHQQ 395
Cdd:PRK06189 318 PELKeGDDFFLVWGGISGGQSTLLVMLTEGyiERGI-PLETIARLLATNPAKRFGLPQKGRLEVGADADFVLVDLDETYT 396
|
410 420 430
....*....|....*....|....*....|....*..
gi 1456770152 396 IIREDVAYKCGWSPFEGRILSgGAVDMTLVNGHVIWN 432
Cdd:PRK06189 397 LTKEDLFYRHKQSPYEGRTFP-GRVVATYLRGQCVYQ 432
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
50-423 |
1.97e-73 |
|
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and dihydroorotase, are involved in the metabolism of pyrimidines and purines, sharing the property of hydrolyzing the cyclic amide bond of each substrate to the corresponding N-carbamyl amino acids. Allantoinases catalyze the degradation of purines, while dihydropyrimidinases and hydantoinases, a microbial counterpart of dihydropyrimidinase, are involved in pyrimidine degradation. Dihydroorotase participates in the de novo synthesis of pyrimidines.
Pssm-ID: 238627 [Multi-domain] Cd Length: 337 Bit Score: 234.21 E-value: 1.97e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 50 KWVIPGMIDDQVHFREPGLT-HKGTIASESAAAVMGGITSFMEMPNVTPPTTTLQALREKFQRASHSSLANYSFYFGA-T 127
Cdd:cd01302 1 LLVLPGFIDIHVHLRDPGGTtYKEDFESGSRAAAAGGVTTVIDMPNTGPPPIDLPAIELKIKLAEESSYVDFSFHAGIgP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 128 NDNLDELKALTASQACGVKVFMGASTGNMLVDDEQILESIFANAPCL---VATHCEHtptikhneetwrarlgdaipage 204
Cdd:cd01302 81 GDVTDELKKLFDAGINSLKVFMNYYFGELFDVDDGTLMRTFLEIASRggpVMVHAER----------------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 205 haairsvdACLtsshqavsLAKKHRTRLHVLHITTADELALFDAAPTLEAlrqkTITTEACVHHLFFNYDDYEMLGHKLK 284
Cdd:cd01302 138 --------AAQ--------LAEEAGANVHIAHVSSGEALELIKFAKNKGV----KVTCEVCPHHLFLDESMLRLNGAWGK 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 285 CNPSVKSSFHQEALWRGVNEGIIDVIATDHAPHLLEEKQ--NDYFAAPSGLPLVQHALPALLDMSSRGIFTPEMVVRKTS 362
Cdd:cd01302 198 VNPPLRSKEDREALWEGVKNGKIDTIASDHAPHSKEEKEsgKDIWKAPPGFPGLETRLPILLTEGVKRGLSLETLVEILS 277
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1456770152 363 HAVAERFQLKDRGYIREGYWADLVVIDPFSHQQIIREDVAYKCGWSPFEGRILSgGAVDMT 423
Cdd:cd01302 278 ENPARIFGLYPKGTIAVGYDADLVIVDPKKEWKVTAEEIESKADWTPFEGMEVT-GKPVST 337
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
20-430 |
2.46e-73 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 235.82 E-value: 2.46e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 20 ADILIDKGRIQKI-ASLIPSRtewQVIDVRGKWVIPGMIDDQVHFREPGLTHKGTIASESAAAVMGGITSFMEMPNVTPP 98
Cdd:PRK04250 15 GGIGIENGRISKIsLRDLKGK---EVIKVKGGIILPGLIDVHVHLRDFEESYKETIESGTKAALHGGITLVFDMPNTKPP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 99 TTTLQALREKFQRASHSSLANYSFYFgATNDNLDELKALTASQAcgvKVFMGASTGNMLVDDeqiLESIFANAPCLVATH 178
Cdd:PRK04250 92 IMDEKTYEKRMRIAEKKSYADYALNF-LIAGNCEKAEEIKADFY---KIFMGASTGGIFSEN---FEVDYACAPGIVSVH 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 179 CEHTPTIKHNEETWRArlgdaipagehAAIRSVDACLTsshqavsLAKKHRTRLHVLHITTADelalfdaapTLEALRQK 258
Cdd:PRK04250 165 AEDPELIREFPERPPE-----------AEVVAIERALE-------AGKKLKKPLHICHISTKD---------GLKLILKS 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 259 TI---TTEACVHHLFFNYDDYEmLGHKLKCNPSVKSSFHQEALWRgvNEGIIDVIATDHAPHLLEEKQndyfAAPSGLPL 335
Cdd:PRK04250 218 NLpwvSFEVTPHHLFLTRKDYE-RNPLLKVYPPLRSEEDRKALWE--NFSKIPIIASDHAPHTLEDKE----AGAAGIPG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 336 VQHALPALLDMSSRGIFTPEMVVRKTSHAVAERFQLKDRGyIREGYWADLVVIDPFSHQQIIREDVAYKCGWSPFEGRIL 415
Cdd:PRK04250 291 LETEVPLLLDAANKGMISLFDIVEKMHDNPARIFGIKNYG-IEEGNYANFAVFDMKKEWTIKAEELYTKAGWTPYEGFKL 369
|
410
....*....|....*
gi 1456770152 416 SGGAVdMTLVNGHVI 430
Cdd:PRK04250 370 KGKVI-MTILRGEVV 383
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
4-431 |
2.01e-63 |
|
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases are a family of enzymes that catalyze the reversible hydrolytic ring opening of the amide bond in five- or six-membered cyclic diamides, like dihydropyrimidine or hydantoin. The hydrolysis of dihydropyrimidines is the second step of reductive catabolism of pyrimidines in human. The hydrolysis of 5-substituted hydantoins in microorganisms leads to enantiomerically pure N-carbamyl amino acids, which are used for the production of antibiotics, peptide hormones, pyrethroids, and pesticides. HYDs are classified depending on their stereoselectivity. This family also includes collapsin response regulators (CRMPs), cytosolic proteins involved in neuronal differentiation and axonal guidance which have strong homology to DHPases, but lack most of the active site residues.
Pssm-ID: 238639 [Multi-domain] Cd Length: 447 Bit Score: 211.31 E-value: 2.01e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 4 LLLTNALIINEDLRYPADILIDKGRIQKIASLIPSRTEWQVIDVRGKWVIPGMIDDQVHFREP--GLTHKGTIASESAAA 81
Cdd:cd01314 1 LIIKNGTIVTADGSFKADILIEDGKIVAIGPNLEAPGGVEVIDATGKYVLPGGIDPHTHLELPfmGTVTADDFESGTRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 82 VMGGITSFMEMPNVTPPTTTLQALREKFQRASHSSLANYSFYFGATNDN---LDELKALTASQACGVKVFMgASTGNMLV 158
Cdd:cd01314 81 AAGGTTTIIDFAIPNKGQSLLEAVEKWRGKADGKSVIDYGFHMIITDWTdsvIEELPELVKKGISSFKVFM-AYKGLLMV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 159 DDEQILESIFA----NApcLVATHCEHTPTIKHNEETWRARlGDAIPAGeHAAIRSVDACLTSSHQAVSLAKKHRTRLHV 234
Cdd:cd01314 160 DDEELLDVLKRakelGA--LVMVHAENGDVIAELQKKLLAQ-GKTGPEY-HALSRPPEVEAEATARAIRLAELAGAPLYI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 235 LHITTADELALFDAAptlealRQK--TITTEACVHHLFFNYDDYE---MLGHKLKCNPSVKSSFHQEALWRGVNEGIIDV 309
Cdd:cd01314 236 VHVSSKEAADEIARA------RKKglPVYGETCPQYLLLDDSDYWkdwFEGAKYVCSPPLRPKEDQEALWDGLSSGTLQT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 310 IATDHAPHLLEEK---QNDYFAAPSGLPLVQHALPALLD-MSSRGIFTPEMVVRKTSHAVAERFQLKDR-GYIREGYWAD 384
Cdd:cd01314 310 VGSDHCPFNFAQKargKDDFTKIPNGVPGVETRMPLLWSeGVAKGRITLEKFVELTSTNPAKIFGLYPRkGTIAVGSDAD 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1456770152 385 LVVIDPFSHQQIIREDVAYKCGWSPFEGRILSgGAVDMTLVNGHVIW 431
Cdd:cd01314 390 LVIWDPNAEKTISADTHHHNVDYNIFEGMKVK-GWPVVTISRGKVVV 435
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
43-417 |
1.30e-62 |
|
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis. This subgroup also contains proteins that lack the active site, like unc-33, a C.elegans protein involved in axon growth.
Pssm-ID: 238642 [Multi-domain] Cd Length: 374 Bit Score: 207.09 E-value: 1.30e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 43 QVIDVRGKWVIPGMIDDQVHFREPGLTHKGTIASESAAAVMGGITSFMEMPNVTPPTTTLQALREKFQRASHSSLANYSF 122
Cdd:cd01317 3 EVIDAEGKILAPGLVDLHVHLREPGFEYKETLESGAKAAAAGGFTTVVCMPNTNPVIDNPAVVELLKNRAKDVGIVRVLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 123 YFGATNDN----LDELKALTASQACGVkvfmgaSTGNMLVDDEQILESIFANAPCL---VATHCEHTPTIKH---NEETW 192
Cdd:cd01317 83 IGALTKGLkgeeLTEIGELLEAGAVGF------SDDGKPIQDAELLRRALEYAAMLdlpIIVHPEDPSLAGGgvmNEGKV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 193 RARLG-DAIP-AGEHAAIRSVdacltsshqaVSLAKKHRTRLHVLHITTADELALFDAAPTLEALrqktITTEACVHHLF 270
Cdd:cd01317 157 ASRLGlPGIPpEAETIMVARD----------LELAEATGARVHFQHLSTARSLELIRKAKAKGLP----VTAEVTPHHLL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 271 FNYDDYEMLGHKLKCNPSVKSSFHQEALWRGVNEGIIDVIATDHAPHLLEEKQNDYFAAPSGLPLVQHALPALL-DMSSR 349
Cdd:cd01317 223 LDDEALESYDTNAKVNPPLRSEEDREALIEALKDGTIDAIASDHAPHTDEEKDLPFAEAPPGIIGLETALPLLWtLLVKG 302
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1456770152 350 GIFTPEMVVRKTSHAVAERFQLkDRGYIREGYWADLVVIDPFSHQQIIREDVAYKCGWSPFEGRILSG 417
Cdd:cd01317 303 GLLTLPDLIRALSTNPAKILGL-PPGRLEVGAPADLVLFDPDAEWIVDEETFRSKSKNTPFDGQKLKG 369
|
|
| PRK01211 |
PRK01211 |
dihydroorotase; Provisional |
21-440 |
1.85e-55 |
|
dihydroorotase; Provisional
Pssm-ID: 179247 [Multi-domain] Cd Length: 409 Bit Score: 189.30 E-value: 1.85e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 21 DILIDKGRIQKIASLIPSRTEwqvIDVRGKwVIPGMIDDQVHFREPGLTHKGTIASESAAAVMGGITSFMEMPNVTPPTT 100
Cdd:PRK01211 17 EIEVEDGKIKSIKKDAGNIGK---KELKGA-ILPAATDIHVHFRTPGETEKEDFSTGTLSAIFGGTTFIMDMPNNNIPIK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 101 TLQALREKFQRASHSSLANYSFYFGATNDNLDELKaltaSQACGVKVFMGAST---GNMLVDDEqiLESIfANAPCLVAT 177
Cdd:PRK01211 93 DYNAFSDKLGRVAPKAYVDFSLYSMETGNNALILD----ERSIGLKVYMGGTTntnGTDIEGGE--IKKI-NEANIPVFF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 178 HCEHTPTIK-HNEETWRARlgdaipagEHAAIRSVDACLTSSHQAVSLAKKHRtrlHVLHITTADELALFdaaptlealr 256
Cdd:PRK01211 166 HAELSECLRkHQFESKNLR--------DHDLARPIECEIKAVKYVKNLDLKTK---IIAHVSSIDVIGRF---------- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 257 qktiTTEACVHHLFFNYDdyeM-LGHKLKCNPSVKSSFHQEALWRGVNEGIIDVIATDHAPHLLEEKQnDYFAAPSGLPL 335
Cdd:PRK01211 225 ----LREVTPHHLLLNDD---MpLGSYGKVNPPLRDRWTQERLLEEYISGRFDILSSDHAPHTEEDKQ-EFEYAKSGIIG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 336 VQHALPALLDMSSRGIFTPEMVVRKTSHAVAERFQLKdRGYIREGYWADLVVIDPFSHQQIIREDVAYKCGWSPFEGril 415
Cdd:PRK01211 297 VETRVPLFLALVKKKILPLDVLYKTAIERPASLFGIK-KGKIEEGYDADFMAFDFTNIKKINDKRLHSKCPVSPFNG--- 372
|
410 420
....*....|....*....|....*
gi 1456770152 416 sggaVDmTLVNGHVIWNGRTIQQKY 440
Cdd:PRK01211 373 ----FD-AIFPSHVIMRGEVVIDNY 392
|
|
| D-hydantoinase |
TIGR02033 |
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ... |
4-431 |
2.00e-54 |
|
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily converts 5,6-dihydrouracil to 3-ureidopropanoate but also acts on dihydrothymine and hydantoin. The enzyme is a metalloenzyme.
Pssm-ID: 273937 [Multi-domain] Cd Length: 454 Bit Score: 187.98 E-value: 2.00e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 4 LLLTNALIINEDLRYPADILIDKGRIQKIASLIPSRTEWQVIDVRGKWVIPGMIDDQVHFREP--GLTHKGTIASESAAA 81
Cdd:TIGR02033 1 LLIKGGTVVNADDVFQADVLIEGGKIVAVGDNLIPPDAVEVIDATGKYVLPGGIDVHTHLEMPfgGTTTADDFFTGTKAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 82 VMGGITSFMEMpNVTPPTTTLQALREKF-QRASHSSLANYSFYFGATNDN---LDELKALTASQacGV---KVFMgASTG 154
Cdd:TIGR02033 81 AAGGTTTIIDF-VVPEKGSSLTEALETWhEKAEGKSVIDYGFHMDITHWNdsvLEEHIPEVKEE--GInsfKVFM-AYKN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 155 NMLVDDEQILESIFA----NApcLVATHCEHTPTIkhNEETWRA-RLGDAIPAGeHAAIRSVDACLTSSHQAVSLAKKHR 229
Cdd:TIGR02033 157 LLMVDDEELFEILKRlkelGA--LLQVHAENGDII--AELQARMlAQGITGPEY-HALSRPPELEAEAVARAITLAALAD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 230 TRLHVLHITTADelalfdAAPTLEALRQK--TITTEACVHHLFFNYDDYE---MLGHKLKCNPSVKSSFHQEALWRGVNE 304
Cdd:TIGR02033 232 APLYVVHVSTKD------AADEIAQARKKgqPVFGETCPQYLVLDDTHYDkpgFEGAKYVCSPPLREPEDQDALWSALSS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 305 GIIDVIATDHAPHLLEEKQ----NDYFAAPSGLPLVQHALPALLD-MSSRGIFTPEMVVRKTSHAVAERFQLKDR-GYIR 378
Cdd:TIGR02033 306 GALQTVGSDHCTFNFAQKKaigkDDFTKIPNGGPGVEERMSLLFDeGVAKGRITLEKFVEVTSTNPAKIFNLYPRkGTIA 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1456770152 379 EGYWADLVVIDPFSHQQIIREDVAYKCGWSPFEGRILSgGAVDMTLVNGHVIW 431
Cdd:TIGR02033 386 VGSDADIVIWDPNRTTVISAETHHSNADYNPFEGFKVR-GAPVSVLSRGRVVV 437
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
4-441 |
1.69e-52 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 182.68 E-value: 1.69e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 4 LLLTNALIINEDLRYPADILIDKGRIQKIASliPSRTEwqVIDVRGKWVIPGMIDDQVHFREP-GlthkGTIASE----- 77
Cdd:PRK08323 3 TLIKNGTVVTADDTYKADVLIEDGKIAAIGA--NLGDE--VIDATGKYVMPGGIDPHTHMEMPfG----GTVSSDdfetg 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 78 SAAAVMGGITSFMEMPnVTPPTTTLQ-ALREKFQRASHSSLANYSFY--FGATNDN-LDELKALTAsqaCGV---KVFMg 150
Cdd:PRK08323 75 TRAAACGGTTTIIDFA-LQPKGQSLReALEAWHGKAAGKAVIDYGFHmiITDWNEVvLDEMPELVE---EGItsfKLFM- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 151 ASTGNMLVDDEQILESIFANAPC--LVATHCEHTPTIKHNEETWRARlGDAIPAGeHAAIRSVDACLTSSHQAVSLAKKH 228
Cdd:PRK08323 150 AYKGALMLDDDELLRALQRAAELgaLPMVHAENGDAIAYLQAKLLAE-GKTGPEY-HALSRPPEVEGEATNRAIMLAELA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 229 RTRLHVLHITTADELALFDAAptlealRQK--TITTEACVHHLFFNYDDYEML----GHKLKCNPSVKSSFHQEALWRGV 302
Cdd:PRK08323 228 GAPLYIVHVSCKEALEAIRRA------RARgqRVFGETCPQYLLLDESEYDGPdwfeGAKYVMSPPLRDKEHQDALWRGL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 303 NEGIIDVIATDHAPHLLEEKQ----NDYFAAPSGLPLVQHALPALLDMS-SRGIFTPEMVVRKTSHAVAERFQLKDR-GY 376
Cdd:PRK08323 302 QDGDLQVVATDHCPFCFEQKKqlgrGDFTKIPNGTPGVEDRMPLLFSEGvMTGRITLNRFVELTSTNPAKIFGLYPRkGT 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1456770152 377 IREGYWADLVVIDPFSHQQIIREDVAYKCGWSPFEGRILSgGAVDMTLVNGHVIWNGRTIQQKYG 441
Cdd:PRK08323 382 IAVGADADIVIWDPNATKTISASTLHSNVDYNPYEGFEVT-GWPVTTLSRGEVVVEDGEFRGKAG 445
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
4-446 |
1.65e-51 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 180.05 E-value: 1.65e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 4 LLLTNALIINEDLRYPADILIDKGRIQKIASLIPSRTewQVIDVRGKWVIPGMIDDQVHFREPGLTHKGTIASESAAAVM 83
Cdd:PRK08044 5 LIIKNGTVILENEARVVDIAVKGGKIAAIGQDLGDAK--EVMDASGLVVSPGMVDAHTHISEPGRSHWEGYETGTRAAAK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 84 GGITSFMEMP-NVTPPTTTLQALREKFQRASHSSLANYSFYFGATNDNLDELKALTASQACGVKVFMgASTGN------- 155
Cdd:PRK08044 83 GGITTMIEMPlNQLPATVDRASIELKFDAAKGKLTIDAAQLGGLVSYNLDRLHELDEVGVVGFKCFV-ATCGDrgidndf 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 156 MLVDDEQILESI--FANAPCLVATHCEHTP-TIKHNEETWRArlgDAIPAGEHAAIRSVDACLTSSHQAVSLAKKHRTRL 232
Cdd:PRK08044 162 RDVNDWQFYKGAqkLGELGQPVLVHCENALiCDELGEEAKRE---GRVTAHDYVASRPVFTEVEAIRRVLYLAKVAGCRL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 233 HVLHITTADELAlfdaaptlEALRQKT----ITTEACVHHLFFNYDDYEMLGHKLKCNPSVKSSFHQEALWRGVNEGIID 308
Cdd:PRK08044 239 HVCHISSPEGVE--------EVTRARQegqdVTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDLENQKGMWEKLFNGEID 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 309 VIATDHAPHLLEEKQNDYFAAPSGLPLVQHALPALLD--MSSRGIFTPeMVVRKTSHAVAERFQLKDRGYIREGYWADLV 386
Cdd:PRK08044 311 CLVSDHSPCPPEMKAGNIMEAWGGIAGLQNCMDVMFDeaVQKRGMSLP-MFGKLMATNAADIFGLQQKGRIAPGKDADFV 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 387 VIDPFSHQQIIREDVAYKCGWSPFEGRILsGGAVDMTLVNGHVIWNgrtiqQKYGLPLEF 446
Cdd:PRK08044 390 FIQPNSSYVLKNEDLEYRHKVSPYVGRTI-GARITKTILRGDVIYD-----IEQGFPVAP 443
|
|
| CAD_DHOase |
cd01316 |
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ... |
53-429 |
5.50e-45 |
|
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate synthetase-aspartate transcarbamoylase-dihydroorotase, which catalyzes the first three steps of de novo pyrimidine nucleotide biosynthesis. Dihydroorotase (DHOase) catalyzes the third step, the reversible interconversion of carbamoyl aspartate to dihydroorotate.
Pssm-ID: 238641 [Multi-domain] Cd Length: 344 Bit Score: 159.92 E-value: 5.50e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 53 IPGMIDDQVHFREPGLTHKGTIASESAAAVMGGITSFMEMPNVTPPTTTLQALREKFQRASHSSLANYSFYFGATNDNLD 132
Cdd:cd01316 5 LPGLIDVHVHLREPGATHKEDFASGTKAALAGGFTMVRAMPNTNPSIVDVASLKLVQSLAQAKARCDYAFSIGATSTNAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 133 ELKALtASQACGVKVFMGAStgnmlvDDEQILESIFAnapclVATHCEHTPTIKhneetwrarlgdaiPAGEHAAIRSVD 212
Cdd:cd01316 85 TVGEL-ASEAVGLKFYLNET------FSTLILDKITA-----WASHFNAWPSTK--------------PIVTHAKSQTLA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 213 ACLTsshqavsLAKKHRTRLHVLHITTADELALFDAAPTlealRQKTITTEACVHHLFFNYDDYEMLGHKLKcnPSVKSS 292
Cdd:cd01316 139 AVLL-------LASLHNRSIHICHVSSKEEINLIRLAKA----RGLKVTCEVSPHHLFLSQDDLPRGQYEVR--PFLPTR 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 293 FHQEALWRgvNEGIIDVIATDHAPHLLEEKQNDyfAAPSGLPLVQHALPALLDMSSRGIFTPEMVVRKTSHAVAERFQLK 372
Cdd:cd01316 206 EDQEALWE--NLDYIDCFATDHAPHTLAEKTGN--KPPPGFPGVETSLPLLLTAVHEGRLTIEDIVDRLHTNPKRIFNLP 281
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1456770152 373 DRgyiregywADLVVIDPFSHQQIIREDVAY-KCGWSPFEGRILSGGaVDMTLVNGHV 429
Cdd:cd01316 282 PQ--------SDTYVEVDLDEEWTIPKNPLQsKKGWTPFEGKKVKGK-VQRVVLRGET 330
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
4-436 |
5.45e-44 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 160.25 E-value: 5.45e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 4 LLLTNALIINEDLRYPADILIDKGRIQKIASLIPSRTEwqVIDVRGKWVIPGMIDDQVHFREP---GLTHKGTIASESAA 80
Cdd:PRK13404 6 LVIRGGTVVTATDTFQADIGIRGGRIAALGEGLGPGAR--EIDATGRLVLPGGVDSHCHIDQPsgdGIMMADDFYTGTVS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 81 AVMGGITSFMEMPNVTPPTTTLQALREKFQRASHSSLANYSFYF---GATNDNL-DELKALTASQACGVKVFMgaSTGNM 156
Cdd:PRK13404 84 AAFGGTTTVIPFAAQHRGQSLREAVEDYHRRAAGKAVIDYAFHLivaDPTEEVLtEELPALIAQGYTSFKVFM--TYDDL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 157 LVDDEQILESIFA--NAPCLVATHCEHTPTIKhneetW-RARLGDAipaGE-----HAAIRSVDACLTSSHQAVSLAKKH 228
Cdd:PRK13404 162 KLDDRQILDVLAVarRHGAMVMVHAENHDMIA-----WlTKRLLAA---GLtapkyHAISRPMLAEREATHRAIALAELV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 229 RTRLHVLHITTADelalfdAAPTLEALRQK--TITTEACVHHLFFNYDDYE---MLGHKLKCNPSVKSSFHQEALWRGVN 303
Cdd:PRK13404 234 DVPILIVHVSGRE------AAEQIRRARGRglKIFAETCPQYLFLTAEDLDrpgMEGAKYICSPPPRDKANQEAIWNGLA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 304 EGIIDVIATDHAPHLLEEKQNDYFAA--------PSGLPLVQHALPALLD-MSSRGIFTPEMVVRKTSHAVAERFQLKDR 374
Cdd:PRK13404 308 DGTFEVFSSDHAPFRFDDTDGKLAAGanpsfkaiANGIPGIETRLPLLFSeGVVKGRISLNRFVALTSTNPAKLYGLYPR 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1456770152 375 -GYIREGYWADLVVIDPFSHQQIIREDVAYKCGWSPFEGRILSGGAVdMTLVNGHVIWNGRTI 436
Cdd:PRK13404 388 kGAIAIGADADIAIWDPDREVTITNADLHHAADYTPYEGMRVTGWPV-TVLSRGRVVVEDGEL 449
|
|
| PLN02795 |
PLN02795 |
allantoinase |
19-444 |
7.94e-41 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 152.24 E-value: 7.94e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 19 PADILIDKGRIQKIASlipsRTEW-------QVIDVRGKWVIPGMIDDQVHFREPGLTHKGTIASESAAAVMGGITSFME 91
Cdd:PLN02795 61 PGAVEVEGGRIVSVTK----EEEApksqkkpHVLDYGNAVVMPGLIDVHVHLNEPGRTEWEGFPTGTKAAAAGGITTLVD 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 92 MP-NVTPPTTTLQALREKFQRASHSSLANYSFYFGATND---NLDELKALTASQACGVKVFMGASTGN--MLVDDEQILE 165
Cdd:PLN02795 137 MPlNSFPSTTSVETLELKIEAAKGKLYVDVGFWGGLVPEnahNASVLEELLDAGALGLKSFMCPSGINdfPMTTATHIKA 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 166 SIFANA----PCLVatHCEHT------PTIKHNEETWRARLGDAIPAGEHAAIRSVdacLTSSHQAVSLAKKHRTRLHVL 235
Cdd:PLN02795 217 ALPVLAkygrPLLV--HAEVVspvesdSRLDADPRSYSTYLKSRPPSWEQEAIRQL---LEVAKDTRPGGVAEGAHVHIV 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 236 HITTADE-LALFDAAPTlealRQKTITTEACVHHLFFNYDDYEMLGHKLKCNPSVKSSFHQEALWRGVNEGIIDVIATDH 314
Cdd:PLN02795 292 HLSDAESsLELIKEAKA----KGDSVTVETCPHYLAFSAEEIPDGDTRYKCAPPIRDAANRELLWKALLDGDIDMLSSDH 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 315 AP-----HLLEEkqNDYFAAPSGLPLVQHALPALLDMSS-RGIfTPEMVVRKTSHAVAERFQLKDRGYIREGYWADLVVI 388
Cdd:PLN02795 368 SPsppdlKLLEE--GNFLRAWGGISSLQFVLPATWTAGRaYGL-TLEQLARWWSERPAKLAGLDSKGAIAPGKDADIVVW 444
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 389 DPFShQQIIREDVAYKCGW---SPFEGRILSgGAVDMTLVNG-HVIWNGRTIQQKYGLPL 444
Cdd:PLN02795 445 DPEA-EFVLDESYPIYHKHkslSPYLGTKLS-GKVIATFVRGnLVFLEGKHAKQACGSPI 502
|
|
| pyrC |
PRK00369 |
dihydroorotase; Provisional |
48-429 |
5.55e-35 |
|
dihydroorotase; Provisional
Pssm-ID: 234738 [Multi-domain] Cd Length: 392 Bit Score: 134.12 E-value: 5.55e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 48 RGKWVIPGMIDDQVHFREPGLTHKGTIASESAAAVMGGITSFMEMPNVTPPTTTLQALREKFQRASHSSLANYSFYFGAT 127
Cdd:PRK00369 41 QGTLILPGAIDLHVHLRGLKLSYKEDVASGTSEAAYGGVTLVADMPNTIPPLNTPEAITEKLAELEYYSRVDYFVYSGVT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 128 ndnlDELKALTASQACGVKVFmgastgnmlVDDEQILESI--FANAPCLVATHCEHTPTIKHNEetwRARLGdaIPAgEH 205
Cdd:PRK00369 121 ----KDPEKVDKLPIAGYKIF---------PEDLEREETFrvLLKSRKLKILHPEVPLALKSNR---KLRRN--CWY-EI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 206 AAIRSVdacltsshqavslakKHRTRLHVLHITTADelalfdaapTLEALRQKTITTEACVHHLFfnyddYEMLGHKL-K 284
Cdd:PRK00369 182 AALYYV---------------KDYQNVHITHASNPR---------TVRLAKELGFTVDITPHHLL-----VNGEKDCLtK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 285 CNPSVKSSFHQEALWRGVNEgiIDVIATDHAPHLLEEKQNDYFAAPSGLPLVQHALPALLDMSSRGIFTPEMVVRKTSHA 364
Cdd:PRK00369 233 VNPPIRDINERLWLLQALSE--VDAIASDHAPHSSFEKLQPYEVCPPGIAALSFTPPFIYTLVSKGILSIDRAVELISTN 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1456770152 365 VAERFQLKDrGYIREGYWADLVVIDpfshqqiiREDVAYKCGWSPFEGRILSG----GAVDMTLVNGHV 429
Cdd:PRK00369 311 PARILGIPY-GEIKEGYRANFTVIQ--------FEDWRYSTKYSKVIETPLDGfelkASVYATIVQGKL 370
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
4-434 |
4.63e-32 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 127.65 E-value: 4.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 4 LLLTNALIINEDLRYPADILIDKGRIQKIASLIPSRTEWQVIDVRGKWVIPGMIDDQVHFREPGLthkGTIASE-----S 78
Cdd:PLN02942 7 ILIKGGTVVNAHHQELADVYVEDGIIVAVAPNLKVPDDVRVIDATGKFVMPGGIDPHTHLAMPFM---GTETIDdffsgQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 79 AAAVMGGITsfMEMPNVTPPTTTLQALREKFQRASHSSLANYSFYFGAT--NDNLD-ELKALTASQAC-GVKVFMgASTG 154
Cdd:PLN02942 84 AAALAGGTT--MHIDFVIPVNGNLLAGYEAYEKKAEKSCMDYGFHMAITkwDDTVSrDMETLVKEKGInSFKFFM-AYKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 155 NMLVDDEQILESiFANAPCLVA---THCEHTPTIKHNEETwRARLGDAIPAGeHAAIRSVDACLTSSHQAVSLAKKHRTR 231
Cdd:PLN02942 161 SLMVTDELLLEG-FKRCKSLGAlamVHAENGDAVFEGQKR-MIELGITGPEG-HALSRPPLLEGEATARAIRLAKFVNTP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 232 LHVLHITTADELalfDAAPTLEALRQKTItTEACVHHLFFN----YDDYEMLGHKLKCNPSVKSSFHQEALWRGVNEGII 307
Cdd:PLN02942 238 LYVVHVMSIDAM---EEIARARKSGQRVI-GEPVVSGLVLDdsklWDPDFTIASKYVMSPPIRPAGHGKALQAALSSGIL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 308 DVIATDHAPHLLEEK---QNDYFAAPSGLPLVQHALPALLD-MSSRGIFTPEMVVRKTSHAVAERFQLKDR-GYIREGYW 382
Cdd:PLN02942 314 QLVGTDHCPFNSTQKafgKDDFRKIPNGVNGIEERMHLVWDtMVESGQISPTDYVRVTSTECAKIFNIYPRkGAILAGSD 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1456770152 383 ADLVVIDPFSHQQIIREDVAYKCGWSPFEGRILSgGAVDMTLVNGHVIW-NGR 434
Cdd:PLN02942 394 ADIIILNPNSTFTISAKTHHSRIDTNVYEGRRGK-GKVEVTISQGRVVWeNGE 445
|
|
| PRK09059 |
PRK09059 |
dihydroorotase; Validated |
1-427 |
1.89e-31 |
|
dihydroorotase; Validated
Pssm-ID: 181631 [Multi-domain] Cd Length: 429 Bit Score: 124.76 E-value: 1.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 1 MKPLLLTNALIIN--EDLRYPADILIDKGRIQKIASLI-----PSRTEwqVIDVRGKWVIPGMIDDQVHFREPGLTHKGT 73
Cdd:PRK09059 2 MRPILLANARIIDpsRGLDEIGTVLIEDGVIVAAGKGAgnqgaPEGAE--IVDCAGKAVAPGLVDARVFVGEPGAEHRET 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 74 IASESAAAVMGGITSFMEMPNvTPPTTTLQALREKFQR-ASHSSLANYsFYFGATNDNL--DELKALTASQACGVKVFmg 150
Cdd:PRK09059 80 IASASRAAAAGGVTSIIMMPD-TDPVIDDVALVEFVKRtARDTAIVNI-HPAAAITKGLagEEMTEFGLLRAAGAVAF-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 151 aSTGNMLVDDEQILESIFANAPCLVATHCEHTPTiKH-------NEETWRARLG-DAIPAGEHAAIRSVDacltsshqaV 222
Cdd:PRK09059 156 -TDGRRSVANTQVMRRALTYARDFDAVIVHETRD-PDlggngvmNEGLFASWLGlSGIPREAEVIPLERD---------L 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 223 SLAKKHRTRLHVLHITTADelalfdaapTLEALRQK-----TITTEACVHHLFFNYDDYEMLGHKLKCNPSVKSSFHQEA 297
Cdd:PRK09059 225 RLAALTRGRYHAAQISCAE---------SAEALRRAkdrglKVTAGVSINHLSLNENDIGEYRTFFKLSPPLRTEDDRVA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 298 LWRGVNEGIIDVIATDHAPHLLEEKQNDYFAAPSGLPLVQHALPALLDMSSRGIFTPEMVVRKTSHAVAERFQLkDRGYI 377
Cdd:PRK09059 296 MVEAVASGTIDIIVSSHDPQDVDTKRLPFSEAAAGAIGLETLLAAALRLYHNGEVPLLRLIEALSTRPAEIFGL-PAGTL 374
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1456770152 378 REGYWADLVVIDPFSHQQIIREDVAYKCGWSPFEGRILSGGAVdMTLVNG 427
Cdd:PRK09059 375 KPGAPADIIVIDLDEPWVVDPEDLKSRSKNTPFEEARFQGRVV-RTIVAG 423
|
|
| PRK07627 |
PRK07627 |
dihydroorotase; Provisional |
20-434 |
7.82e-28 |
|
dihydroorotase; Provisional
Pssm-ID: 181059 [Multi-domain] Cd Length: 425 Bit Score: 114.39 E-value: 7.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 20 ADILIDKGRIQKIASLIPSRTEWQVIDVRGKWVIPGMIDDQVHFREPGLTHKGTIASESAAAVMGGITSFMEMPNVTPPt 99
Cdd:PRK07627 21 ADLYVAAGKIAAIGQAPAGFNADKTIDASGLIVCPGLVDLSARLREPGYEYKATLESEMAAAVAGGVTSLVCPPDTDPV- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 100 ttlqaLRE-------KFqRASHSSLANY----SFYFGATNDNLDELKALTASqACgvkvfMGASTGNMLVDDEQIL---- 164
Cdd:PRK07627 100 -----LDEpglvemlKF-RARNLNQAHVyplgALTVGLKGEVLTEMVELTEA-GC-----VGFSQANVPVVDTQVLlral 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 165 --ESIFANAPCLVAthcehtptikhnEETWRARLGDAiPAGEHAAiR------SVDACLTSSHQAVSLAKKHRTRLHVLH 236
Cdd:PRK07627 168 qyASTFGFTVWLRP------------LDAFLGRGGVA-ASGAVAS-RlglsgvPVAAETIALHTIFELMRVTGARVHLAR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 237 ITTADELALFDAAPTlEALrqkTITTEACVHHLFFNYDDYEMLGHKLKCNPSVKSSFHQEALWRGVNEGIIDVIATDHAP 316
Cdd:PRK07627 234 LSSAAGVALVRAAKA-EGL---PVTCDVGVNHVHLIDVDIGYFDSQFRLDPPLRSQRDREAIRAALADGTIDAICSDHTP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 317 HLLEEKQNDYFAAPSGLPLVQHALPALLDMSSR-GIFTPEMVVRKTSHAvAERFQLKdRGYIREGYWADLVVIDPFSHQQ 395
Cdd:PRK07627 310 VDDDEKLLPFAEATPGATGLELLLPLTLKWADEaKVPLARALARITSAP-ARVLGLP-AGRLAEGAPADLCVFDPDAHWR 387
|
410 420 430
....*....|....*....|....*....|....*....
gi 1456770152 396 IIREDVAYKCGWSPFEGRILSgGAVDMTLVNGHVIWNGR 434
Cdd:PRK07627 388 VEPRALKSQGKNTPFLGYELP-GRVRATLVAGQVAFERR 425
|
|
| PRK07369 |
PRK07369 |
dihydroorotase; Provisional |
20-390 |
6.94e-23 |
|
dihydroorotase; Provisional
Pssm-ID: 236002 [Multi-domain] Cd Length: 418 Bit Score: 100.06 E-value: 6.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 20 ADILIDKGRIQKIASLI-PSRTEWQVIDVRGkWVI-PGMIDDQVHFREPGLTHKGTIASESAAAVMGGITSFMEMPNVTP 97
Cdd:PRK07369 22 ADVLIEDGKIQAIEPHIdPIPPDTQIIDASG-LILgPGLVDLYSHSGEPGFEERETLASLAAAAAAGGFTRVAILPDTFP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 98 PT---TTLQALREKFQRASHSSLanysFYFGA-TNDN----LDELKALTASQACGvkvFM-GASTGNM-----LVDDEQI 163
Cdd:PRK07369 101 PLdnpATLARLQQQAQQIPPVQL----HFWGAlTLGGqgkqLTELAELAAAGVVG---FTdGQPLENLallrrLLEYLKP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 164 LESIFANAPClvathcehTPTIKHN----EETWRARLG-DAIPA-GEHAAIRSVdacltsshqaVSLAKKHRTRLHVLHI 237
Cdd:PRK07369 174 LGKPVALWPC--------DRSLAGNgvmrEGLLALRLGlPGDPAsAETTALAAL----------LELVAAIGTPVHLMRI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 238 TTADELALFDAAPTlealRQKTITTEACVHHLFFNYDDYEMLGHKLKCNPSVKSSFHQEALWRGVNEGIIDVIATDHAPH 317
Cdd:PRK07369 236 STARSVELIAQAKA----RGLPITASTTWMHLLLDTEALASYDPNLRLDPPLGNPSDRQALIEGVRTGVIDAIAIDHAPY 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1456770152 318 LLEEKQNDYFAAPSG---LPLvqhALPALLD-MSSRGIFTPEMVVRKTSHAVAERFQLKDRGyIREGYWADLVVIDP 390
Cdd:PRK07369 312 TYEEKTVAFAEAPPGaigLEL---ALPLLWQnLVETGELSALQLWQALSTNPARCLGQEPPS-LAPGQPAELILFDP 384
|
|
| PRK08417 |
PRK08417 |
metal-dependent hydrolase; |
22-427 |
6.99e-18 |
|
metal-dependent hydrolase;
Pssm-ID: 236262 [Multi-domain] Cd Length: 386 Bit Score: 85.14 E-value: 6.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 22 ILIDKGRIQKIASLIPSRtewQVIDVRGKWVIPGMIDDQVHFREPGLTHKgTIASESAAAVMGGITSFMEMPNVTPPTTT 101
Cdd:PRK08417 1 IRIKDGKITEIGSDLKGE---EILDAKGKTLLPALVDLNVSLKNDSLSSK-NLKSLENECLKGGVGSIVLYPDSTPAIDN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 102 LQALrEKFQRASHSSLANY--SFYFGATNDNLDELKALTASQACGVkvFMGASTGNMLVddEQILE-SIFANAPCLVatH 178
Cdd:PRK08417 77 EIAL-ELINSAQRELPMQIfpSIRALDEDGKLSNIATLLKKGAKAL--ELSSDLDANLL--KVIAQyAKMLDVPIFC--R 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 179 CEHTPTIKH---NEETWRARLGdaipagehaaIRSVDACLTSSHQA--VSLAKKHRTRLHVLHITTADELALFDAAPTLE 253
Cdd:PRK08417 150 CEDSSFDDSgvmNDGELSFELG----------LPGIPSIAETKEVAkmKELAKFYKNKVLFDTLALPRSLELLDKFKSEG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 254 AlrqkTITTEACVHHLFFNYDDYEMLGHKLKCNPSVKSSFHQEALWRGVNEGIIDVIATDHAPHLLEEKQNDYFAAPSGL 333
Cdd:PRK08417 220 E----KLLKEVSIHHLILDDSACENFNTAAKLNPPLRSKEDRLALLEALKEGKIDFLTSLHSAKSNSKKDLAFDEAAFGI 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 334 PLVQHALPALLD-MSSRGIFTPEMVVRKTSHAVAErFQLKDRGYIREGYWADLVVIDPfsHQQIIREDvaykcGWSPFEG 412
Cdd:PRK08417 296 DSICEYFSLCYTyLVKEGIITWSELSRFTSYNPAQ-FLGLNSGEIEVGKEADLVLFDP--NESTIIDD-----NFSLYSG 367
|
410
....*....|....*
gi 1456770152 413 RILSgGAVDMTLVNG 427
Cdd:PRK08417 368 DELY-GKIEAVIIKG 381
|
|
| COG3653 |
COG3653 |
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ... |
4-434 |
9.29e-15 |
|
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442870 [Multi-domain] Cd Length: 528 Bit Score: 76.37 E-value: 9.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 4 LLLTNALII----NEdlRYPADILIDKGRIQKIASLIPSRTEwQVIDVRGKWVIPGMIDdqVH-------FREPGLTHKG 72
Cdd:COG3653 4 LLIRGGTVVdgtgAP--PFRADVAIKGGRIVAVGDLAAAEAA-RVIDATGLVVAPGFID--IHthydlqlLWDPRLEPSL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 73 T-----------------IASESAAAVMGGITSFMEMPNVTPPT-TTLQALREKFQRASHSslANYSFYFG--------- 125
Cdd:COG3653 79 RqgvttvvmgncgvsfapVRPEDRDRLIDLMEGVEGIPEGLDWDwESFGEYLDALERRGLG--VNVASLVGhgtlrayvm 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 126 ------ATNDNLDELKALTAsQA--CGvkvFMGASTGnmlvddeqiLESIfanaPCLVATHcehtptikhnEEtwRARLG 197
Cdd:COG3653 157 glddrpPTPEELARMRALLR-EAmeAG---ALGLSTG---------LIYV----PGTYAST----------DE--LVALA 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 198 DAipAGEH-----AAIRSVDACLTSSHQ-AVSLAKKHRTRLHVLHITTADE---LALFDAAPTLEALRQK---------- 258
Cdd:COG3653 208 KV--VAEYggvyqSHMRDEGDGLLEAVDeLIRIGREAGVPVHISHLKAAGKpnwGKADEVLALIEAARAEgldvtadvyp 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 259 ---TITTEACVHHLFFNYDDYEMLGHKLKcNPSVKSSFHQEalwrgVNEGIIDVIATDHAPHLLEEKQNDYFAAPSGLPL 335
Cdd:COG3653 286 ypaGSTGLGALLPPWAAAGGLDERLARLR-DPATRARIRAE-----IEEGLPDNLLGRGGWDNILISDSPPNEPLVGKSL 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 336 VQ-------HALPALLDM-------------------------------SS--------------------------RGI 351
Cdd:COG3653 360 AEiaaergvDPADAALDLlleedgrvlivyfimseedvrellrhpwvmiGSdgglggkahpraygtfprvlghyvreRGV 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 352 FTPEMVVRKTSHAVAERFQLKDRGYIREGYWADLVVIDPfshqQIIREDVAYKcgwSPFEgriLSGGaVDMTLVNGHVIW 431
Cdd:COG3653 440 LSLEEAVRKLTSLPADRLGLKDRGLLRPGYRADLVVFDP----ATLADRATFD---LPAQ---RADG-IRAVIVNGVVVV 508
|
....
gi 1456770152 432 -NGR 434
Cdd:COG3653 509 eDGK 512
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
51-430 |
8.50e-14 |
|
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase superfamily. The family includes Adenine deaminase EC:3.5.4.2 that hydrolyses adenine to form hypoxanthine and ammonia. Adenine deaminases reaction is important for adenine utilization as a purine and also as a nitrogen source. This family also includes dihydroorotase and N-acetylglucosamine-6-phosphate deacetylases, EC:3.5.1.25 These enzymes catalyze the reaction N-acetyl-D-glucosamine 6-phosphate + H2O <=> D-glucosamine 6-phosphate + acetate. This family includes the catalytic domain of urease alpha subunit. Dihydroorotases (EC:3.5.2.3) are also included.
Pssm-ID: 460401 [Multi-domain] Cd Length: 334 Bit Score: 72.15 E-value: 8.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 51 WVIPGMIDDQVHFREPGLTHKGTIASESA--------AAVMGGITSFMEMPNVTPptTTLQALREkfqrASHSSLANYSF 122
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLRGIPVPPEFAYealrlgitTMLKSGTTTVLDMGATTS--TGIEALLE----AAEELPLGLRF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 123 YFGATndNLDELKALTASQACGVKVFMGASTgnMLVDDEQILESIFANAPCLVAThcehTPTIKH-NEETWRARLGDAIP 201
Cdd:pfam01979 75 LGPGC--SLDTDGELEGRKALREKLKAGAEF--IKGMADGVVFVGLAPHGAPTFS----DDELKAaLEEAKKYGLPVAIH 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 202 AGEHAAIrsvdacltsshQAVSLAKKHRTRLHVLHITTADELALFDaaptlealrqktITTEACVHHLFFNYDDYEMLGH 281
Cdd:pfam01979 147 ALETKGE-----------VEDAIAAFGGGIEHGTHLEVAESGGLLD------------IIKLILAHGVHLSPTEANLLAE 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 282 KLK-------CNPSVKSSFHQEALWRGVNEGIIDVIATDHAPHlleekqNDYFAAPSGLPLVqhalpALLDMSSRGIFTP 354
Cdd:pfam01979 204 HLKgagvahcPFSNSKLRSGRIALRKALEDGVKVGLGTDGAGS------GNSLNMLEELRLA-----LELQFDPEGGLSP 272
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1456770152 355 EMVVRKTSHAVAERFQLKDR-GYIREGYWADLVVIDPFshqqiIREDVAYkcgwspfegrILSGGAVDMTLVNGHVI 430
Cdd:pfam01979 273 LEALRMATINPAKALGLDDKvGSIEVGKDADLVVVDLD-----PLAAFFG----------LKPDGNVKKVIVKGKIV 334
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
4-433 |
8.69e-13 |
|
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of N-acyl-D-amino acids to produce the corresponding D-amino acids, which are used as intermediates in the synthesis of pesticides, bioactive peptides, and antibiotics.
Pssm-ID: 238622 [Multi-domain] Cd Length: 415 Bit Score: 69.63 E-value: 8.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 4 LLLTNALIIneD----LRYPADILIDKGRIQKIASLIPSRTEwQVIDVRGKWVIPGMID-----DQVHFREPGLTHK--- 71
Cdd:cd01297 2 LVIRNGTVV--DgtgaPPFTADVGIRDGRIAAIGPILSTSAR-EVIDAAGLVVAPGFIDvhthyDGQVFWDPDLRPSsrq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 72 G--TI----ASESAAAV-----------MGGITSFMEMPNVTPPTTT--LQALrEKFQRAshsslANYSFYFG------- 125
Cdd:cd01297 79 GvtTVvlgnCGVSPAPAnpddlarlimlMEGLVALGEGLPWGWATFAeyLDAL-EARPPA-----VNVAALVGhaalrra 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 126 --------ATNDNLDELKALTA-SQACGvkvFMGASTGNmlvddeqilesifANAPCLVATHCEhtptikhneetwraRL 196
Cdd:cd01297 153 vmgldareATEEELAKMRELLReALEAG---ALGISTGL-------------AYAPRLYAGTAE--------------LV 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 197 GDAIPAGEHAAIRS--VDACLTSSHQA----VSLAKKHRTRLHVLHITTADELALFDAAPTLEALRqktittEACVHHLF 270
Cdd:cd01297 203 ALARVAARYGGVYQthVRYEGDSILEAldelLRLGRETGRPVHISHLKSAGAPNWGKIDRLLALIE------AARAEGLQ 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 271 FNYDDYemlghklkcnPSVKSSFHQEALW--RGVNEGIIDVIATDHaPHLleekqndyfAAPSGLPLVqhalpaLLDMS- 347
Cdd:cd01297 277 VTADVY----------PYGAGSEDDVRRImaHPVVMGGSDGGALGK-PHP---------RSYGDFTRV------LGHYVr 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 348 SRGIFTPEMVVRKTSHAVAERFQLKDRGYIREGYWADLVVIDPfshqqiirEDVAYKcgwSPFEGRILSGGAVDMTLVNG 427
Cdd:cd01297 331 ERKLLSLEEAVRKMTGLPARVFGLADRGRIAPGYRADIVVFDP--------DTLADR---ATFTRPNQPAEGIEAVLVNG 399
|
....*.
gi 1456770152 428 HVIWNG 433
Cdd:cd01297 400 VPVVRD 405
|
|
| DHOase |
cd01294 |
Dihydroorotase (DHOase) catalyzes the reversible interconversion of carbamoyl aspartate to ... |
53-340 |
5.21e-12 |
|
Dihydroorotase (DHOase) catalyzes the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in the pyrimidine biosynthesis. In contrast to the large polyfunctional CAD proteins of higher organisms, this group of DHOases is monofunctional and mainly dimeric.
Pssm-ID: 238619 Cd Length: 335 Bit Score: 66.54 E-value: 5.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 53 IPGMIDDQVHFREPGLTHK--GTIASESAAAVMggitsfmeMPNVTPPTTTLQAL---REKFQRASHSSLANY--SFYFg 125
Cdd:cd01294 3 IPRPDDMHLHLRDGAMLKLvlPYTARGFSRAIV--------MPNLKPPVTTTADAlayRERILAADPGPNFTPlmTLYL- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 126 atNDNLDELKALTASQAC---GVKVFMGASTGNmlvdDEQILESIFANAPCLVATHCEHTPTIKHNEETwrarlgdaipa 202
Cdd:cd01294 74 --TENTTPEELREAKKKGgirGVKLYPAGATTN----SQGGVTDLEKIYPVLEAMQKLGMPLLVHGEVP----------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 203 geHAAIRSVDA---CLTSSHQavsLAKKHrTRLHVL--HITTADELALFDAAPTLEAlrqKTITTeacvHHLFFNYDDye 277
Cdd:cd01294 137 --DFKIDVLDReakFIPVLEP---LAQRF-PKLKIVleHITTADAVEYVKSCNENVA---ATITP----HHLLLTRDD-- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 278 MLGHKLK----CNPSVKSSFHQEALwrgvnegiIDVIA---------TDHAPHLLEEKQNDY-----FAAPSGLPLVQHA 339
Cdd:cd01294 202 LLGGGLNphlyCKPVAKRPEDREAL--------RKAATsghpkfflgSDSAPHPKSNKESSCgcagiFSAPIALPYLAEV 273
|
.
gi 1456770152 340 L 340
Cdd:cd01294 274 F 274
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
1-93 |
9.37e-11 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 63.06 E-value: 9.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 1 MKPLLLTNALII---NEDLRYPADILIDKGRIQKI--ASLIPSRTEWQVIDVRGKWVIPGMIDDQVHF-----REPGLTH 70
Cdd:COG1228 7 AGTLLITNATLVdgtGGGVIENGTVLVEDGKIAAVgpAADLAVPAGAEVIDATGKTVLPGLIDAHTHLglgggRAVEFEA 86
|
90 100 110
....*....|....*....|....*....|...
gi 1456770152 71 KGTIASES----------AAAVMGGITSFMEMP 93
Cdd:COG1228 87 GGGITPTVdlvnpadkrlRRALAAGVTTVRDLP 119
|
|
| COG3964 |
COG3964 |
Predicted amidohydrolase [General function prediction only]; |
3-62 |
7.04e-10 |
|
Predicted amidohydrolase [General function prediction only];
Pssm-ID: 443164 [Multi-domain] Cd Length: 376 Bit Score: 60.57 E-value: 7.04e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1456770152 3 PLLLTNALIINED--LRYPADILIDKGRIQKIASLIPSRTEWQVIDVRGKWVIPGMIDDQVH 62
Cdd:COG3964 1 DLLIKGGRVIDPAngIDGVMDIAIKDGKIAAVAKDIDAAEAKKVIDASGLYVTPGLIDLHTH 62
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
4-62 |
1.75e-09 |
|
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl group of N-acetyl-glucosamine-6-phosphate (GlcNAc-6-P) to glucosamine 6-phosphate and acetate. This is the first committed step in the biosynthetic pathway to amino-sugar-nucleotides, which is needed for cell wall peptidoglycan and teichoic acid biosynthesis. Deacetylation of N-acetylglucosamine is also important in lipopolysaccharide synthesis and cell wall recycling.
Pssm-ID: 238434 [Multi-domain] Cd Length: 374 Bit Score: 59.13 E-value: 1.75e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1456770152 4 LLLTNALIINEDLRYPADILIDKGRIQKIASLIPSRTEWQVIDVRGKWVIPGMIDDQVH 62
Cdd:cd00854 1 LIIKNARILTPGGLEDGAVLVEDGKIVAIGPEDELEEADEIIDLKGQYLVPGFIDIHIH 59
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
4-62 |
9.29e-09 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 57.17 E-value: 9.29e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1456770152 4 LLLTNALIIN--EDLRYPADILIDKGRIQKIASLIPSRTEWQVIDVRGKWVIPGMIDDQVH 62
Cdd:PRK09237 1 LLLRGGRVIDpaNGIDGVIDIAIEDGKIAAVAGDIDGSQAKKVIDLSGLYVSPGWIDLHVH 61
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
4-431 |
4.16e-08 |
|
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and metabolism, General function prediction only]; Cytosine/adenosine deaminase or related metal-dependent hydrolase is part of the Pathway/BioSystem: Pyrimidine salvage
Pssm-ID: 440171 [Multi-domain] Cd Length: 416 Bit Score: 55.22 E-value: 4.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 4 LLLTNALII--NEDLRY--PADILIDKGRIQKI---ASLIPSRTEWQVIDVRGKWVIPGMID-----DQVHFR------- 64
Cdd:COG0402 2 LLIRGAWVLtmDPAGGVleDGAVLVEDGRIAAVgpgAELPARYPAAEVIDAGGKLVLPGLVNththlPQTLLRgladdlp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 65 ------------EPGLTHKGTIASESAAAV---MGGITSFMEMPNVTPPTT--TLQALREKFQRASHSslanysfyfgat 127
Cdd:COG0402 82 lldwleeyiwplEARLDPEDVYAGALLALAemlRSGTTTVADFYYVHPESAdaLAEAAAEAGIRAVLG------------ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 128 ndnldelkaltasqacgvKVFMGASTGNMLVDDEqilESIFANAPCLVATHcehtptikHNEETWRARLGDAIpageHAA 207
Cdd:COG0402 150 ------------------RGLMDRGFPDGLREDA---DEGLADSERLIERW--------HGAADGRIRVALAP----HAP 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 208 IRSVDACLTsshQAVSLAKKHRTRLHVlHI-TTADE----LALFDAAPT-----LEALRQKTItteaCVHHLFFNYDDYE 277
Cdd:COG0402 197 YTVSPELLR---AAAALARELGLPLHT-HLaETRDEvewvLELYGKRPVeyldeLGLLGPRTL----LAHCVHLTDEEIA 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 278 MLG-------HklkcNPSvkSSF--------HQEALWRGVNEGI-IDVIATDHAPHLLEE-KQNDYFAAPSGLPlvQHAL 340
Cdd:COG0402 269 LLAetgasvaH----CPT--SNLklgsgiapVPRLLAAGVRVGLgTDGAASNNSLDMFEEmRLAALLQRLRGGD--PTAL 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 341 PA--LLDMSSRGiftpemvvrktshaVAERFQLKDR-GYIREGYWADLVVIDPfshqqiirEDVAYKCGWSPFEGRILSG 417
Cdd:COG0402 341 SAreALEMATLG--------------GARALGLDDEiGSLEPGKRADLVVLDL--------DAPHLAPLHDPLSALVYAA 398
|
490
....*....|....*.
gi 1456770152 418 G--AVDMTLVNGHVIW 431
Cdd:COG0402 399 DgrDVRTVWVAGRVVV 414
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
5-62 |
6.75e-08 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 54.33 E-value: 6.75e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1456770152 5 LLTNALIINED-LRYPADILIDKGRIQKIASLIPSRTEwqVIDVRGKWVIPGMIDDQVH 62
Cdd:COG1820 1 AITNARIFTGDgVLEDGALLIEDGRIAAIGPGAEPDAE--VIDLGGGYLAPGFIDLHVH 57
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
4-437 |
1.34e-06 |
|
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. Atrazine, a chlorinated herbizide, can be catabolized by a variety of different bacteria. The first three steps of the atrazine dehalogenation pathway are catalyzed by atrazine chlorohydrolase (AtzA), hydroxyatrazine ethylaminohydrolase (AtzB), and N-isopropylammelide N-isopropylaminohydrolase (AtzC). All three enzymes belong to the superfamily of metal dependent hydrolases. AtzA and AtzB, beside other related enzymes are represented in this CD.
Pssm-ID: 238623 [Multi-domain] Cd Length: 411 Bit Score: 50.28 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 4 LLLTNALIINEDLRYP---ADILIDKGRIQKIASLIPSRTEW--QVIDVRGKWVIPGMIDDQVHF--------------- 63
Cdd:cd01298 1 ILIRNGTIVTTDPRRVledGDVLVEDGRIVAVGPALPLPAYPadEVIDAKGKVVMPGLVNTHTHLamtllrgladdlplm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 64 --------REPGLT--HKGTIASESAAAVM--GGITSFMEMpnvtpptttlqalrekfqrashsslanYSFYFGATNDnl 131
Cdd:cd01298 81 ewlkdliwPLERLLteEDVYLGALLALAEMirSGTTTFADM---------------------------YFFYPDAVAE-- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 132 delkaltASQACGVKVFMGASTGNMLVDDEQILESIFANAPCLVATHcehtptikhnEETWRARLGDAIpaGEHAAIRSV 211
Cdd:cd01298 132 -------AAEELGIRAVLGRGIMDLGTEDVEETEEALAEAERLIREW----------HGAADGRIRVAL--APHAPYTCS 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 212 DACLTsshQAVSLAKKHRTRLHvLHIT-TADELALFDAA---PTLEALRQ------KTItteaCVHHLFFNYDDYEMLG- 280
Cdd:cd01298 193 DELLR---EVAELAREYGVPLH-IHLAeTEDEVEESLEKygkRPVEYLEElgllgpDVV----LAHCVWLTDEEIELLAe 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 281 ------HklkcNPSvkSSFH--------QEALWRGVNEGiidvIATDHAP-----HLLEE------KQNDYFAAPSGLPl 335
Cdd:cd01298 265 tgtgvaH----NPA--SNMKlasgiapvPEMLEAGVNVG----LGTDGAAsnnnlDMFEEmrlaalLQKLAHGDPTALP- 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 336 vqhalpalldmssrgiftPEMVVRKTSHAVAERFQLKDRGYIREGYWADLVVIDP--FSHQQI--IREDVAYKCGwspfe 411
Cdd:cd01298 334 ------------------AEEALEMATIGGAKALGLDEIGSLEVGKKADLILIDLdgPHLLPVhdPISHLVYSAN----- 390
|
490 500
....*....|....*....|....*.
gi 1456770152 412 grilsGGAVDMTLVNGHVIWNGRTIQ 437
Cdd:cd01298 391 -----GGDVDTVIVNGRVVMEDGELL 411
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
4-95 |
2.40e-06 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 49.71 E-value: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 4 LLLTNALIIN----EdlRYPADILIDKGRIQKIASLIPSRTEwqVIDVRGKWVIPGMIDDQVHFrEPGLThkgTIASESA 79
Cdd:COG1001 7 LVIKNGRLVNvftgE--ILEGDIAIAGGRIAGVGDYIGEATE--VIDAAGRYLVPGFIDGHVHI-ESSMV---TPAEFAR 78
|
90 100
....*....|....*....|
gi 1456770152 80 AAVMGGITSFM----EMPNV 95
Cdd:COG1001 79 AVLPHGTTTVIadphEIANV 98
|
|
| ureC |
PRK13308 |
urease subunit alpha; Reviewed |
4-147 |
1.30e-05 |
|
urease subunit alpha; Reviewed
Pssm-ID: 183965 [Multi-domain] Cd Length: 569 Bit Score: 47.39 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 4 LLLTNALIINEDLRY-PADILIDKGRIQKIA-------------SLI--PSRTewqVIDVRGKWVIPGMIDDQVHFREPG 67
Cdd:PRK13308 70 FVLCNVTVIDPVLGIvKGDIGIRDGRIVGIGkagnpdimdgvdpRLVvgPGTD---VRPAEGLIATPGAIDVHVHFDSAQ 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 68 LTHKgtiasesaaAVMGGITSFMEM---PNVTPPTTTLQALrEKFQRASHSSLANYSFYFGATNDNLDELKALTASQACG 144
Cdd:PRK13308 147 LVDH---------ALASGITTMLGGglgPTVGIDSGGPFNT-GRMLQAAEAWPVNFGFLGRGNSSKPAALIEQVEAGACG 216
|
...
gi 1456770152 145 VKV 147
Cdd:PRK13308 217 LKI 219
|
|
| Urease_alpha |
cd00375 |
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis ... |
4-147 |
5.20e-05 |
|
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis of urea to form ammonia and carbon dioxide. Nickel-dependent ureases are found in bacteria, fungi and plants. Their primary role is to allow the use of external and internally generated urea as a nitrogen source. The enzyme consists of 3 subunits, alpha, beta and gamma, which can be fused and present on a single protein chain and which in turn forms multimers, mainly trimers. The large alpha subunit is the catalytic domain containing an active site with a bi-nickel center complexed by a carbamylated lysine. The beta and gamma subunits play a role in subunit association to form the higher order trimers.
Pssm-ID: 238221 [Multi-domain] Cd Length: 567 Bit Score: 45.40 E-value: 5.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 4 LLLTNALIINEDLRYPADILIDKGRIQKIAS--------------LIPSRTEwqVIDVRGKWVIPGMIDDQVHFREPGLT 69
Cdd:cd00375 67 LVITNALIIDYTGIYKADIGIKDGRIVAIGKagnpdimdgvtpnmIVGPSTE--VIAGEGKIVTAGGIDTHVHFICPQQI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 70 hkgtiasesAAAVMGGITSFM-------EMPNVTPPTTTLQALREKFQRASHSSLaNYSFYFGATNDNLDELKALTASQA 142
Cdd:cd00375 145 ---------EEALASGITTMIgggtgpaAGTKATTCTPGPWNIKRMLQAADGLPV-NIGFLGKGNGSSPDALAEQIEAGA 214
|
....*
gi 1456770152 143 CGVKV 147
Cdd:cd00375 215 CGLKL 219
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
21-62 |
1.76e-04 |
|
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238632 [Multi-domain] Cd Length: 338 Bit Score: 43.47 E-value: 1.76e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1456770152 21 DILIDKGRIQKIASLIPSRTEWQVIDVRGKWVIPGMIDDQVH 62
Cdd:cd01307 1 DVAIENGKIAAVGAALAAPAATQIVDAGGCYVSPGWIDLHVH 42
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
4-62 |
3.04e-04 |
|
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of the degradative pathway to eliminate proteins with beta-L-isoaspartyl peptide bonds, bonds whereby the beta-group of an aspartate forms the peptide link with the amino group of the following amino acid. Formation of this bond is a spontaneous nonenzymatic reaction in nature and can profoundly effect the function of the protein. Isoaspartyl dipeptidase is an octameric enzyme that contains a binuclear zinc center in the active site of each subunit and shows a strong preference of hydrolyzing Asp-Leu dipeptides.
Pssm-ID: 238633 [Multi-domain] Cd Length: 387 Bit Score: 42.76 E-value: 3.04e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1456770152 4 LLLTNALIINEDLRYPADILIDKGRIQKIASLIPSRTEW--QVIDVRGKWVIPGMIDDQVH 62
Cdd:cd01308 2 TLIKNAEVYAPEYLGKKDILIAGGKILAIEDQLNLPGYEnvTVVDLHGKILVPGFIDQHVH 62
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
1-58 |
3.32e-04 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 42.86 E-value: 3.32e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1456770152 1 MKPLLLTNALIINEDLRYPADILIDKGRIQKIASliPSRTEWQVIDVRGKWVIPGMID 58
Cdd:PRK15446 1 MMEMILSNARLVLPDEVVDGSLLIEDGRIAAIDP--GASALPGAIDAEGDYLLPGLVD 56
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
1-73 |
3.69e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 42.68 E-value: 3.69e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1456770152 1 MKPLLLTNALIINEDLRYP----ADILIDKGRIQKIASLIPSrTEWQVIDVRGKWVIPGMIDDQVHFREPGLTHKGT 73
Cdd:PRK08204 1 MKRTLIRGGTVLTMDPAIGdlprGDILIEGDRIAAVAPSIEA-PDAEVVDARGMIVMPGLVDTHRHTWQSVLRGIGA 76
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
4-62 |
8.74e-04 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 41.52 E-value: 8.74e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1456770152 4 LLLTNALII--NEDLRYP-ADILIDKGRIQKIASLIPSRTEWQVIDVRGKWVIPGMIDDQVH 62
Cdd:PRK07228 3 ILIKNAGIVtmNAKREIVdGDVLIEDDRIAAVGDRLDLEDYDDHIDATGKVVIPGLIQGHIH 64
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
5-62 |
1.20e-03 |
|
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) catalyze the deamination of cytosine, producing uracil and ammonia. They play an important role in pyrimidine salvage. CDs are present in prokaryotes and fungi, but not mammalian cells. The bacterial enzymes, but not the fungal enzymes, are related to the adenosine deaminases (ADA). The bacterial enzymes are iron dependent and hexameric.
Pssm-ID: 238618 [Multi-domain] Cd Length: 398 Bit Score: 41.08 E-value: 1.20e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1456770152 5 LLTNALIINEDLRyPADILIDKGRIQKIASLIPSRTEWQVIDVRGKWVIPGMIDDQVH 62
Cdd:cd01293 1 LLRNARLADGGTA-LVDIAIEDGRIAAIGPALAVPPDAEEVDAKGRLVLPAFVDPHIH 57
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
4-69 |
1.22e-03 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 41.32 E-value: 1.22e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1456770152 4 LLLTNALII--NEDLRYPADILIDKGRI------QKIASLIPSRTEwqVIDVRGKWVIPGMIDDQVHFREPGLT 69
Cdd:COG1574 10 LLLTNGRIYtmDPAQPVAEAVAVRDGRIvavgsdAEVRALAGPATE--VIDLGGKTVLPGFIDAHVHLLGGGLA 81
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
296-389 |
1.31e-03 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 41.24 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 296 EALWRGVNEGIIDVIA--TD--HAPHLLEEKQNDYfaapsglpLVQHALPALLDmssrgiftPEMVVRKTSHAVAERFQL 371
Cdd:COG1001 240 PALLPAVTELNSRRCAlcTDdrHPDDLLEEGHIDH--------VVRRAIELGLD--------PVTAIQMATLNAAEHFGL 303
|
90
....*....|....*...
gi 1456770152 372 KDRGYIREGYWADLVVID 389
Cdd:COG1001 304 KDLGAIAPGRRADIVLLD 321
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
1-63 |
1.91e-03 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 40.30 E-value: 1.91e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1456770152 1 MKPLLLTNALIINEDlryPADILIDKGRIQKIASLIPSRTEWQVIDVRGKWVIPGMIDDQVHF 63
Cdd:PRK05985 1 MTDLLFRNVRPAGGA---AVDILIRDGRIAAIGPALAAPPGAEVEDGGGALALPGLVDGHIHL 60
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
21-182 |
2.03e-03 |
|
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. The Arabidopsis homolog LAF3 has been identified as a factor required for phytochrome A signalling.
Pssm-ID: 238625 [Multi-domain] Cd Length: 479 Bit Score: 40.37 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 21 DILIDKGRI------QKIASLIPSRTewQVIDVRGKWVIPGMIDDQVHFrepglthkgtiasesaaaVMGGItsFMEMPN 94
Cdd:cd01300 1 AVAVRDGRIvavgsdAEAKALKGPAT--EVIDLKGKTVLPGFIDSHSHL------------------LLGGL--SLLWLD 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 95 VTPPTTTLQAL-REKFQRASHSSlANYSFYFGATNDNLDELKALTAsqacgvkvfmgastgnmlvddeQILESIFANAPC 173
Cdd:cd01300 59 LSGVTSKEEALaRIREDAAAAPP-GEWILGFGWDESLLGEGRYPTR----------------------AELDAVSPDRPV 115
|
....*....
gi 1456770152 174 LVATHCEHT 182
Cdd:cd01300 116 LLLRRDGHS 124
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
16-63 |
4.87e-03 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 39.02 E-value: 4.87e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1456770152 16 LRYPAD--ILIDKGRI------QKIASLIPSRTEwqVIDVRGKWVIPGMIDDQVHF 63
Cdd:PRK09228 26 LRYIEDglLLVEDGRIvaagpyAELRAQLPADAE--VTDYRGKLILPGFIDTHIHY 79
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
4-62 |
5.91e-03 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 38.71 E-value: 5.91e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1456770152 4 LLLTNALII--NEDLR-YPADILIDKGRIQKIASLIPSRTEwqVIDVRGKWVIPGMIDDQVH 62
Cdd:PRK06380 3 ILIKNAWIVtqNEKREiLQGNVYIEGNKIVYVGDVNEEADY--IIDATGKVVMPGLINTHAH 62
|
|
| ureC |
PRK13207 |
urease subunit alpha; Reviewed |
4-90 |
6.44e-03 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237305 [Multi-domain] Cd Length: 568 Bit Score: 39.00 E-value: 6.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1456770152 4 LLLTNALIINEDLRYPADILIDKGRIQKIAS------------LIPSRTEwqVIDVRGKWVIPGMIDDQVHFrepglthk 71
Cdd:PRK13207 69 TVITNALILDHWGIVKADIGIKDGRIVAIGKagnpdiqdgvdiIIGPGTE--VIAGEGLIVTAGGIDTHIHF-------- 138
|
90 100
....*....|....*....|
gi 1456770152 72 gtIASESA-AAVMGGITSFM 90
Cdd:PRK13207 139 --ICPQQIeEALASGVTTMI 156
|
|
| PRK07572 |
PRK07572 |
cytosine deaminase; Validated |
1-62 |
9.79e-03 |
|
cytosine deaminase; Validated
Pssm-ID: 181039 Cd Length: 426 Bit Score: 38.08 E-value: 9.79e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1456770152 1 MKPLLLTNALIinEDLRYPADILIDKGRIQKIASLIPSRTEwQVIDVRGKWVIPGMIDDQVH 62
Cdd:PRK07572 1 MFDLIVRNANL--PDGRTGIDIGIAGGRIAAVEPGLQAEAA-EEIDAAGRLVSPPFVDPHFH 59
|
|
| |
